31st Annual Student Research Conference
Expression and Purification of Disulfide Bond Forming Enzyme
Courtney R. Bingham* and Kerstin E. Peterson
Dr. Cassidy Dobson, Faculty Mentor
Disulfide bond forming enzyme (DBF), found in the hyperthermophilic bacteria Sulfolobus solfataricus, has been demonstrated to correct improperly formed disulfide bonds. Improper disulfide bonding can lead to protein misfolding and protein aggregation diseases such as Alzheimer’s, Parkinson’s, and ALS. In order to understand the mechanism of DBF, the first step in evaluating its application to protein misfolding diseases is protein production. DBF is over-expressed in E. coli using the induction sugar rhamnose and purified by column chromatography in order to obtain pure, concentrated DBF protein. The extent of this purification is then evaluated by SDS-PAGE before further testing of its potential activity and uses.
Keywords: protein, protein purification, SDS-PAGE, protein expression
Topic(s):Chemistry
Biology
Presentation Type: Poster
Session: 4-2
Location: GEO - SUB
Time: 3:30